1gct: Difference between revisions

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[[Image:1gct.gif|left|200px]]
{{Seed}}
[[Image:1gct.png|left|200px]]


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{{STRUCTURE_1gct|  PDB=1gct  |  SCENE=  }}  
{{STRUCTURE_1gct|  PDB=1gct  |  SCENE=  }}  


'''IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?'''
===IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?===




==Overview==
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Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., &amp; Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.
The line below this paragraph, {{ABSTRACT_PUBMED_2819046}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 2819046 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2819046}}


==About this Structure==
==About this Structure==
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[[Category: Dixon, M M.]]
[[Category: Dixon, M M.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
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